6DGV
iGABASnFR Fluorescent GABA Sensor precursor
Summary for 6DGV
| Entry DOI | 10.2210/pdb6dgv/pdb |
| Descriptor | Fluorescent GABA Sensor precursor (2 entities in total) |
| Functional Keywords | gaba binding protein, fluorescent sensor, superfolder, circularly permuted gfp, periplasmic binding protein, fluorescent protein |
| Biological source | Pseudomonas fluorescens |
| Total number of polymer chains | 1 |
| Total formula weight | 62633.34 |
| Authors | Marvin, J.S.,Looger, L.L. (deposition date: 2018-05-18, release date: 2019-04-03, Last modification date: 2024-10-30) |
| Primary citation | Marvin, J.S.,Shimoda, Y.,Magloire, V.,Leite, M.,Kawashima, T.,Jensen, T.P.,Kolb, I.,Knott, E.L.,Novak, O.,Podgorski, K.,Leidenheimer, N.J.,Rusakov, D.A.,Ahrens, M.B.,Kullmann, D.M.,Looger, L.L. A genetically encoded fluorescent sensor for in vivo imaging of GABA. Nat.Methods, 16:763-770, 2019 Cited by PubMed Abstract: Current techniques for monitoring GABA (γ-aminobutyric acid), the primary inhibitory neurotransmitter in vertebrates, cannot follow transients in intact neural circuits. To develop a GABA sensor, we applied the design principles used to create the fluorescent glutamate receptor iGluSnFR. We used a protein derived from a previously unsequenced Pseudomonas fluorescens strain and performed structure-guided mutagenesis and library screening to obtain intensity-based GABA sensing fluorescence reporter (iGABASnFR) variants. iGABASnFR is genetically encoded, detects GABA release evoked by electric stimulation of afferent fibers in acute brain slices and produces readily detectable fluorescence increases in vivo in mice and zebrafish. We applied iGABASnFR to track mitochondrial GABA content and its modulation by an anticonvulsant, swimming-evoked, GABA-mediated transmission in zebrafish cerebellum, GABA release events during interictal spikes and seizures in awake mice, and found that GABA-mediated tone decreases during isoflurane anesthesia. PubMed: 31308547DOI: 10.1038/s41592-019-0471-2 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.8 Å) |
Structure validation
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